Abstract
The receptors that mediate vision at night are the rods which, as mentioned earlier, contain a pigment—visual purple or rhodopsin—responsible for the absorption of light in the primary photochemical event leading to sensation. According to the photochemist, then, the visual process consists of the absorption of light by a specialized molecule, visual purple or rhodopsin. The absorption of light provides the rhodopsin molecule with a supply of extra energy and it is said, in this state, to be ‘activated’. In this activated state it is highly unstable and so it will change to a new form, i.e. the molecule will undergo some kind of chemical change by virtue of this absorption of energy. The effects of this change will be to cause an ‘excited’ condition of the rod as a whole and it will be this excited condition that will ultimately lead to the sensation of light.
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References
Abrahamson, E. W. & Ostroy, S. E. (1967) The photochemical and macromolecular aspects of vision. Progr. Biophys. 17, 181–215.
Abrahamson, E. W. & Wiesenweld, J. R. (1972), The structure, spectra, and reactivity of visual pigments. Hdb. Sensory Physiol. 7/1, 69–121.
Adler, A. J. & Evans, C. D. (1985) Some functional characteristics of purified bovine interphotoreceptor retinol-binding protein. Invest. Ophthal. 26, 273–282.
Adler, A. J. & Martin, K. J. (1982) Retinol binding proteins in bovine interphotoreceptor matrix. Biochem. Biophys. Res. Commun. 108, 1601.
Allen, D. M. & McFarland, W. N. (1973) The effect of temperature on rhodopsin-porphyropsin ratios in a fish. Vision Res. 13, 1303–1309.
Alvarez, R. A., Bridges, C. D. B. & Fong, S.-L. (1981) High-pressure liquid chromatography of fatty acid esters of retinol isomers. Invest. Ophthal. 20, 304–313.
Amer, S. & Akhtar, M. (1972) The regeneration of rhodopsin from all-trans retinal: Solubilization of enzyme system involved in the completion of the visual cycle. Biochem. J. 128, 987–989.
Amer, S. & Akhtar, M. (1973) Studies on the regeneration of rhodopsin from all-trans retinal in isolated rat retinae. Nature 245, 221–223.
Anderson, D. H. & Fisher, S. K. (1976) The photoreceptors of diurnal squirrels; outer segment structure, disc shedding and protein renewal. J. Ultrastr. Res. 55, 119–141.
Anderson, D. H., Fisher, S. K., Erickson, P. A. & Tabor, G. A. (1980) Rod and cone disc shedding in the rhesus monkey retina: a quantiative study. Exp. Eye Res. 30, 559–574.
Azuma, K., Azuma, M. & Sickel, W. (1977) Regeneration of rhodopsin in frog rod outer segments. J. Physiol. 271, 747–759.
Bairati, A. & Orzalesi, N. (1963) The ultrastructure of the pigment epithelium and of the photoreceptor-pigment epithelium junction. J. Ultrastr. Res. 9, 484–496.
Basinger, S., Bok, D. & Hall, M. (1976) Rhodopsin in the rod outer segment plasma membrane. J. Cell Biol. 69, 29–42.
Baumann, C. (1970) Regeneration of rhodopsin in the isolated retina of the frog (Rana esculenta). Vision Res. 10, 627–637.
Beatty, D. D. (1975) Visual pigments of the American eel Anguilla rostrata. Vision Res. 15, 771–776.
Bernstein, S. A., Breding, D. J. & Fisher, S. K. (1984) The influence of light on cone disk shedding in the lizard, Sceloporus occidentalis. J. Cell Biol. 99, 379–389.
Besharse, J. C. & Pfenninger, K. H. (1980) Membrane assembly in retinal photoreceptors I. Freeze-fracture analysis of cytoplasmic vesicles in relationship to disc assembly. J. Cell Biol. 87, 451–463.
Bibb, C. & Young, R. W. (1974) Renewal of glycerol in the visual cells and pigment epithelium of the frog retina. J. Cell Biol. 62, 378–389.
Blasie, J. K. & Worthington, C. R. (1969) Planar liquid-like arrangement of photopigment molecule in frog retinal receptor disk membranes. J. Mol. Biol. 39, 417–439.
Blazynski, C. & Ostroy, S. E. (1984) Pathways in the hydrolysis of vertebrate rhodopsin. Vision Res. 24, 459–470.
Bok, D. (1985) Retinal photoreceptor-pigment epithelium interactions. Invest. Ophthal. 26, 1659–1694.
Bok, D. & Hall, M. D. (1971) The role of the pigment epithelium in the etiology of inherited retinal dystrophy in the rat. J. Cell Biol. 49, 664–682.
Bok, D. & Heller, J. (1976) Transport of retinol from the blood to the retina: an autoradiographic study of the pigment epithelial cell surface receptor for plasma retinol-binding protein. Exp. Eye Res. 22, 395–402.
Bok, D., Ong, D. E. & Chytil, F. (1984) Immunocytochemical localization of cellular retinol binding protein in the rat retina. Invest. Ophthal. 25, 877–883.
Bok, D. & Young, R. W. (1972) The renewal of diffusely distributed protein in the outer segments of rods and cones. Vision Res. 12, 161–168.
Borggreven, J. M. P. M., Rotmans, J. P., Bonting, S. L. & Daemen, F. J. M. (1971) The role of phospholipids in cattle rhodopsin studied with phospholipase C. Arch. Biochem. Biophys. 145, 290–299.
Bowmaker, J. K. & Martin, G. R. (1984) Colour vision in the penguin, Spheniscus humboldti: a microspectrofluorometric study. Vision Res. 24, 1702 (Abstr.).
Bownds, D. (1967) Site of attachment of retinal in rhodopsin. Nature 216, 1178–1181.
Bridges, C. D. B. (1961) Studies on the flash photolysis of visual pigments. Biochem. J. 79, 128–134.
Bridges, C. D. B. (1964) The distribution of visual pigments in freshwater fishes. Abstr. Fourth Internat. Congr. Photobiol., Oxford, p. 53. Bucks: Beacon Press.
Bridges, C. D. B. (1972) The rhodopsin-porphyropsin system. In: Handbook of Sensory Physiology. VII/1, pp. 417–486. Springer: Berlin.
Bridges, C. D. B. (1976) Vitamin A and the role of the pigment epithelium during bleaching and regeneration of rhodopsin in the frog eye. Exp. Eye Res. 22, 435–455.
Bridges, C. D. B., Alvarez, R. A., Fong, S.-L., Gonzalez-Fernandez, F., Lam, D. K. & Liou, G. I. (1984) Visual cycle in the mammalian eye. Retinoid binding protein and the distribution of 11-cis retinoids. Vision Res. 24, 1581–1594.
Bunt-Milam, A. H. & Saari, J. C. (1983) Immunocytochemical localization of two retinoid-binding proteins in vertebrate retina. J. Cell Biol. 97, 703–712.
Chader, G. J. & Wiggert, B. (1984) Interophotoreceptor retinoid-binding protein. Characteristics in bovine and monkey. Vision Res. 24, 1605–1614.
Chader, G. J., Wiggert, B., Lai, Y.-L., Lee, L. & Fletcher, R. T. (1983) Interophotoreceptor retinol-binding protein: a possible role in retinoid transport in the retina. Progr. Ret. Res. 2, 163–189.
Cohen, D. & Nir, I. (1983) Cytochemical evaluation of anionic sites on the surface of cultured pigment epithelium cells from normal and dystrophic RCS rats. Exp. Eye Res. 37, 575–582.
Collins, F. D. & Morton, R. A. (1950) Studies on rhodopsin. I–III. Biochem. J. 47, 3–9, 10–17, 18–24.
Crescitelli, F. (1985) Some properties of solubilized human rhodopsin. Exp. Eye Res. 40, 521–535.
Crescitelli, F. & Dartnall, H. J. A. (1953) Human visual purple. Nature 172, 195–196.
Daemen, F. J. M., Rotmans, J. P. & Bonting, S. L. (1974) On the rhodopsin cycle. Exp. Eye Res. 18, 97–103.
Danielli, J. F. & Davson, H. (1935) A contribution to the theory of permeability of thin films. J. cell. comp. Physiol. 5, 495.
Dartnall, H. J. A. (1957) The Visual Pigments. London: Methuen.
Dartnall, H. J. A., Lander, M. R. & Munz, F. W. (1961) Periodic changes in the visual pigment of a fish. In Progress in Photobiology, pp. 203–213. Amsterdam, Elsevier.
Dartnall, H. J. A. & Lythgoe, J. N. (1965) The spectral clustering of visual pigments. Vision Res. 5, 81–100.
Davison, M. D. & Findlay, J. B. C. (1986) Modification of ovine opsin with photosensitive hydrophobic probe 1-azide-4-[125I] iodobenzene. Labelling of the chromophore-attachment domain. Biochem. J. 234, 413–420.
DeFoe, D. M. & Bok, D. (1983) Rhodopsin chromophore exchanges among opsin molecules in the dark. Invest. Ophthal. 24, 1211–1226.
DeGrip, W. J., Bonting, S. L. & Daeman, F. J. M. (1973) The binding site of retinaldehyde in cattle rhodopsin. Biochim. biophys. Acta 303, 189–193.
DeGrip, W. J., Van de Laar, G. L. M., Daemen, F. J. M. & Bonting, S. L. (1973) Biochemical aspects of the visual process. XXIII. Biochim. biophys. Acta 325, 315–322.
Denton, E. J. (1959) The contribution of the photosensitive and other molecules to the absorption of whole retina. Proc. Roy. Soc., B 150, 78–94.
Denton, E. J. & Warren, F. J. (1956) Visual pigments of deep sea fish. Nature 178, 1059.
Ditto, M. (1975) A difference between developing rods and cones in the formation of the outer segment membranes. Vision Res. 15, 535–536.
Dowling, J. E. (1960) Chemistry of visual adaptation in the rat. Nature 188, 114–118.
Dowling, J. E. & Hubbard, R. (1963) Effect of brilliant flashes on light and dark adaptation. Nature 199, 972–975.
Fager, L. Y. & Fager, R. S. (1981) Chicken blue and chicken violet, short wavelength sensitive visual pigments. Vision Res. 21, 581–586.
Fager, R. S., Sejnowski, P. & Abrahamson, E. W. (1972) Aqueous cyanohydridoborate reduction of the rhodopsin chromophore. Biochem. Biophys. Res. Comm. 47, 1244–1247.
Frank, R. N. (1969) Photoproducts of rhodopsin bleaching in the isolated, perfused frog retina. Vision Res. 9, 1415–1433.
Fukuda, M. N., Papermaster, D. S. & Hargrave, P. A. (1979) Rhodopsin carbohydrate. Structure of small oligosaccharides attached at two sites near the NH2 terminus. J. Biol. Chem. 254, 8201–8207.
Gonzalez-Fernandez, F., Fong, S.-L., Liou, I. & Bridges, C. D. B. (1985) Intetstitial retinal-binding protein (IRBP) in the RCS rat: effect of dark-rearing. Invest. Ophthal. 26, 1381–1385.
Hagins, W. A. (1956) Flash photolysis of rhodopsin in the retina. Nature 177, 989–990.
Hargrave, P. A. et al. (1983) The structure of bovine rhodopsin. Biophys. Struct. Mech. 9, 235–241. (Quoted by Hargrave et al., 1984.)
Hargrave, P. A., McDowell, J. H., Feldmann, R. J., Atkinson, P. H., Rao, J. K. M. & Argos, P. (1984) Rhodopsin’s protein and carbohydrate structure: selected aspects. Vision Res. 24, 1487–1499.
Harosi, F. I. & MacNichol, E. F. (1974) Visual pigments of goldfish cones. Spectral properties and dichroism. J. gen. Physiol. 63, 279–304.
Heller, J. (1968) Purification, molecular weight, and composition of bovine visual pigment. Biochem. 7, 2906–2913.
Heller, J. (1975) Interactions of plasma retinol-binding protein with its receptor. J. Biol. Chem. 250, 3613–3619.
Heller, J. & Bok, D. (1976) Transport of retinol from the blood to the retina: involvement of high molecular weight lipoproteins as intracellular carriers. Exp. Eye Res. 22, 403–410.
Herman, K. G. & Steinberg, R. H. (1982) Phagosome movement and the diurnal pattern of phagocytosis in the tapetal retinal pigment epithelium of the opossum. Invest. Ophthal. 23, 277–290.
Hogan, M. J. & Wood, I. (1974) Phagocytosis by pigment epitheium of human retinal cones. Nature 252, 305–307.
Hollyfield, J. G., Fliesler, S. J., Rayborn, M. E., Fong, S. L., Landers, R. A. & Bridges, C. D. B. (1985) Synthesis and secretion of interstitial retinol-binding protein by the human retina. Invest. Ophthal. 26, 58–67.
Huang, P. T., Spira, A. W. & Wyse, J. P. H. (1982) Phagocytosis in the fetal pigment epithelium: evidence for cyclic activity. Invest, Ophthal. 22, 428–438.
Hubbard, R. & Colman, A. D. (1959) Vitamin A content of the frog eye during light and dark adaptation. Science 130, 977–978.
Hubbard, R. & Kropf, A. (1959) Molecular aspects of visual excitation. Ann. N.Y. Acad. Sci. 81, 388–398.
Hubbard, R. & Wald, G. (1952) Cis-trans isomers of vitamin A and retinene in the rhodopsin system. J. gen. Physiol. 36, 269–315.
Jancsó, N. & Jancsó, H. (1936) Fluoreszenmikroskopische Beobachtung der reversiblen Vitamin-Bildung in der Netzhaut während des Sehaktes. Biochem. Z. 287, 289–290.
Jan, L. Y. & Revel, J.-P. (1974) Ultrastructural localization of rhodopsin in the vertebrate retina. J. Cell Biol. 62, 257–263.
Knowles, A. & Dartnall, H. J. A. (1977) The Photobiology of Vision. Vol. 2B, The Eye (Ed. Davson, H.). Academic Press, New York and London.
Köttgen, E. & Abelsdorff, G. (1896) Absorption und Zersetzung des Sehpurpurs bei den Wirbeltieren. Z. Psychol. Physiol. Sinnesorg. 12, 161–184.
Lai, Y.-L., Wiggert, B., Liu, Y. P. & Chader, G. J. (1982). Interphotoreceptor retinol-binding proteins: possible transport vehicles between compartments of the retina. Nature 298, 848.
La Vail, M. M. (1976) Rod outer segment disc shedding in relation to cyclic lighting. Exp. Eye Res. 23, 277–280.
Liang, C.-J., Yamashita, K., Muellenberg, C. G., S¢hichi, H. & Kobata, A. (1979) Structure of the carbohydrate moieties of bovine rhodopsin. J. Biol. Chem. 254, 6414–6418.
Liebman, P. A. & Entine, G. (1968) Visual pigments of frog and tadpole (Rana pipiens). Vision Res. 8, 761–775.
Liebman, P. A., Jagger, W. S., Kaplan, M. W. & Bargoot, F. G. (1974) Membrane structure changes in rod outer segments associated with rhodopsin bleaching. Nature 251, 31–36.
Liou, G. I., Bridges, C. D. B., Fong, S.-L., Alvarez, R. A. & Gonzalez-Fernandez, F. (1982) Vitamin A transport between retina and pigment epithelium—an interstitial protein carrying endogenous retino (interstitial retinol-binding protein). Vision Res. 22, 1457–1467.
Long, K. O., Fisher, S. K., Fariss, R. N. & Anderson, D. H. (1986) Disc shedding and autophagy in the cone-dominant ground squirrel retina. Exp. Eye Res. 43, 193–205.
Lythgoe, J. N. (1979) The Ecology of Vision. Clarendon Press: Oxford.
Lythgoe, J. N. (1984) Visual pigments and environmental light. Vision Res. 24, 1539–1550.
Lythgoe, R. J. (1937) Absorption spectra of visual purple and visual yellow. J. Physiol. 89, 331–358.
Lythgoe, R. J. & Quilliam, J. P. (1938) The relation of transient orange to visual purple and indicator yellow. J. Physiol. 94, 399–410.
Maraini, G. & Gozzoli, F. (1975) Binding of retinol to isolated retinal pigment epithelium in the presence and absence of retinol-binding protein. Invest. Ophthal. 14, 785–787.
Mathies, R., Oseroff, A. R. & Stryer, L. (1976) Rapid flow resonance Raman spectroscopy of photolabile molecules: rhodopsin and isorhodopsin. Proc. Nat. Acad. Sci. Wash. 73, 1–5.
McFarland, W. N. & Munz, F. W. (1975) The evolution of photopic visual pigments in fishes. Vision Res. 15, 1071–1080.
Muntz, W. R. A. & Mouat, G. S. V. (1984) Annual variations in the visual pigments of brown trout inhabiting lochs providing different light environments. Vision Res. 24, 1575–1580.
Muntz, W. R. A. & Reuter, T. (1966) Visual pigments and spectral sensitivity in Rana temporaria and other European tadpoles. Vision Res. 6, 601–618.
Munz, F. W. (1958) Photosensitive pigments from the retinae of certain deep-sea fishes. J. Physiol. 140, 220–235.
Nathans, J. & Hogness, D. S. (1983) Isolation, sequence analysis and intron-exon arrangement of the gene encoding bovine rhodopsin. Cell 34, 807–814.
Nilsson, S. E. G. (1964) Receptor cell outer segment development and ultra-structure of the disk membranes in the retina of the tadpole (Rana pipiens). J. Ultrastr. Res. 11, 581–620.
Nir, I. & Papermaster, D. S. (1983) Differential distribution of opsin in the plasma membrane of frog photoreceptors: an immunocytochemical study. Invest. Ophthal. 24, 868.
Ohtsu, K., Naito, K. & Wilt, F. H. (1966) Metabolic basis of visual pigment conversion in metamorphosing Rana catesbiana. Dev. Biol. 10, 216–232.
Ovchinnikov, Y. A. et al. (1982) The complete amino acid sequence of visual rhodopsin. Biorg. Khim. 8, 1011–1014.
Papermaster, D. S., Converse, C. A. & Siu, J. (1975) Membrane biosynthesis in the frog retina: opsin transport in the photoreceptor cell. Biochemistry 14, 1343–1352.
Paulsen, R., Miller, J. A., Brodie, A. E. & Bownds, M. D. (1975) The decay of long-lived photoproducts in the isolated bullfrog rod outer segment: relationship to other dark reactions. Vision Res. 15, 1325–1332.
Peters, K., Applebury, M. L. & Rentzepis, P. M. (1977) Primary photochemical event in vision: proton translocation. Proc. Nat. Acad. Sci. 74, 3119–3123.
Peters, K.-R., Palade, G. E., Schneider, B. G. & Papermaster, D. S. (1983) Fine structure of a periciliary ridge complex of frog retinal rod cells revealed by ultrahigh resolution scanning electron microscopy. J. Cell Biol. 96, 265–276.
Pfeffer, B., Wiggert, B., Lee, L., Zonnenberg, B., Newsome, D. & Chader, G. J. (1983) The presence of a soluble inter-photoreceptor retinoid-binding protein in the retinal inter-photoreceptor space. J. Cell Physiol. 117, 333.
Poincelot, R. P., Millar, P. G., Kimbel, R. L. & Abrahamson, E. W. (1969) Lipid to protein chromophore transfer in the photolysis of visual pigments. Nature 221, 256–257.
Poo, M. M. & Cone, R. A. (1973) Lateral diffusion of rhodopsin in Necturus rods. Exp. Eye Res. 17, 503–510.
Pugh, E. N. (1975) Rhodopsin flash photolysis in man. J. Physiol. 248, 393–412.
Richardson, T. M. (1969) Cytoplasmic and ciliary connections between the inner and outer segments of mammalian visual receptors. Vision Res. 9, 727–731.
Ripps, H., Mehaffey, L. & Siegel, I. M. (1981) Rhodopsin kinetics in the cat retina. J. Gen. Physiol. 77, 317–334.
Ripps, H. & Weale, R. A. (1969) Flash bleaching of rhodopsin in the human retina. J. Physiol. 200, 151–159.
Rotmans, J. P., Daemen, F. J. M. & Bonting, S. L. (1974) Biochemical aspects of the visual process. XXVI. Binding site and migration of retinaldehyde during rhodopsin photolysis. Biochim. biophys. Acta 357, 151–158.
Saari, J. C., Bunt-Milam, A. H., Bredberg, L. & Garwin, G. G. (1984) Properties and immunocytochemical localization of three retinoid-binding proteins from bovine retina. Vision Res. 24, 1595–1603.
Schwanzara, S. A. (1967) The visual pigments of freshwater fishes. Vision Res. 7, 121–148.
Spitznas, M. & Hogan, M. J. (1970) Outer segments of photoreceptors and the retinal pigment epithelium. Arch. Ophthal. 84, 810–819.
Steinberg, R. H., Wood, I. & Hogan, M. J. (1977) Pigment epithelial ensheathment and phagocytosis of extrafoveal cones in human retina. Phil. Trans. 277, 459–476.
Tabor, G. A., Fisher, S. K. & Anderson, D. H. (1979) Evidence for a circadian rhythm of disc shedding in light-entrained gray squirrels. ARVO Suppl. 18, 81.
Tabor, G. A., Fisher, S. K. & Anderson, D. H. (1980) Rod and cone disc shedding in light-entrained tree squirrels. Exp. Eye Res. 30, 545–557.
Tamai, M., Teirstein, P., Goldman, A., O’Brien, P. & Chader, G. (1978) The pineal gland does not control rod outer segment shedding and phagocytosis in the rat retina and pigment epithelium. Invest. Ophthal. 17, 558–562.
Thompson, P. & Findlay, J. B. (1984) Phosphorylation of ovine rhodopsin. Identification of the phosphorylated sites. Biochem. J. 220, 773–780.
Trayhurn, P. & Habgood, J. O. (1975) The effect of trypsin on the retinal rod outer segments: trypsin digestion as a means of isolating viable discs. Exp. Eye Res. 20, 479–487.
Tsinn, A. T. C. & Beatty, D. D. (1977) Visual pigment changes in rainbow trout in response to temperature. Science 195, 1358–1360.
Tsinn, A. T. C. & Beattey, D. D. (1978) Goldfish rhodopsin: P4991. Vision Res. 18, 1453–1455.
Wald, G. (1935) Carotenoids and the visual cycle. J. gen. Physiol. 19, 351–371.
Wald, G. (1939) The porphyropsin visual system. J. gen. Physiol. 22, 775–794.
Wald, G. (1946) The chemical evolution of vision. Harvey Lectures 41, 148–152.
Wald, G. (1960) The distribution and evolution of visual systems. In Comparative Biochemistry, vol. I. New York: Academic Press.
Wald, G. & Brown, P. K. (1952) The role of sulphydryl groups in the bleaching and synthesis of rhodopsin. J. gen. Physiol. 35, 797–821.
Wiggert, B. O. & Chader, G.J. (1975) A receptor for retinol in the developing retina and pigment epithelium. Exp. Eye Res. 21, 143–151.
Wiggert, B., Lee, L., O’Brien, P. J. & Chader, G. J. (1984) Synthesis of interphotoreceptor retinol-binding protein (IRBP) by monkey retina in organ culture: effect of monensin. Biochem. Biophys. Res. Comm. 118, 789–796.
Wiggert, B., Lee, L., Rodriguez, M., Hess, H., Redmond, T.M. & Chader, G. J. (1986) Immunochemical distribution of inter-photoreceptor retinoid—bindging protein in selected species. Invest. Ophthal., 27, 1041–1049.
Wilt, F. H. (1959) The differentiation of visual pigments in metamorphosing larvae of Rana catesbiana. Dev. Biol. 1, 199–233.
Wong, J. K. & Ostroy, S. E. (1973) Hydrogen ion changes of rhodopsin. I. Proton uptake during the metarhodopsin I478 metarhodopsin II308 reactions. Arch. Biochem. Biophys. 154, 1–7.
Worthington, C. R. (1973) X-ray analysis of retinal photoreceptor structure. Exp. Eye Res. 17, 487–501.
Wu, C.-W. & Stryer, L. (1972) Proximity relationships in rhodopsin. Proc. Nat. Acad. Sci. Wash. 69, 1104–1108.
Yoshizawa, T. (1972) The behaviour of visual pigments at low temperatures. Hdb. Sensory Physiol. 7(1), 146–179.
Yoshizawa, T., Schishida, Y. & Matsuoka, S. (1984) Primary intermediates of rhodopsin studied by low temperature spectrophotometry and laser photolysis. Vision Res. 24, 1455–1463.
Young, R. W. (1971) Shedding of discs from rod outer segments in the rhesus monkey. J. Ultrastr. Res. 34, 190–203.
Young, R. W. (1972) The daily rhythm of shedding and degradation of cone outer segment membranes in the lizard retina. J. Ultrastr. Res. 61, 172–185.
Young, R. W. (1976) Visual cells and the concept of renewal. Invest. Ophthal. 15, 700–725.
Zimmerman, W. F. (1974) The distributions and proportions of vitamin A compounds during the visual cycle in the rat. Vision Res. 14, 795–802.
Zimmerman, W. F., Lion, R., Daemen, F. J. M., & Bonting, S. L. (1975) Distribution of specific retinol dehydrogenase activities in sub-cellular fractions of bovine retina and pigment epithelium. Exp. Eye Res. 21, 325–332.
Zorn, M. (1974) The effect of blocked sulfhydryl groups on the regenerability of bleached rhodopsin. Exp. Eye. Res. 19, 215–221.
Zorn, M. & Futterman, S. (1971) Properties of rhodopsin dependent upon associated phospholipid. J. biol. Chem. 246, 881–886.
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Davson, H. (1990). Photochemical Aspects of Vision. In: Physiology of the Eye. Palgrave, London. https://doi.org/10.1007/978-1-349-09997-9_8
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